Abstract
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
| Original language | English |
|---|---|
| Pages (from-to) | 7868-7869 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 132 |
| Issue number | 23 |
| DOIs | |
| Publication status | Published - 2010 Jun 16 |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
Cite this
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Helix formation in preorganized β/γ-peptide foldamers : Hydrogen-bond analogy to the α-helix without α-amino acid residues. / Guo, Li; Almeida, Aaron M.; Zhang, Weicheng; Reidenbach, Andrew G.; Choi, Soo Hyuk; Guzei, Ilia A.; Gellman, Samuel H.
In: Journal of the American Chemical Society, Vol. 132, No. 23, 16.06.2010, p. 7868-7869.Research output: Contribution to journal › Article
TY - JOUR
T1 - Helix formation in preorganized β/γ-peptide foldamers
T2 - Hydrogen-bond analogy to the α-helix without α-amino acid residues
AU - Guo, Li
AU - Almeida, Aaron M.
AU - Zhang, Weicheng
AU - Reidenbach, Andrew G.
AU - Choi, Soo Hyuk
AU - Guzei, Ilia A.
AU - Gellman, Samuel H.
PY - 2010/6/16
Y1 - 2010/6/16
N2 - We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
AB - We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
UR - http://www.scopus.com/inward/record.url?scp=77953314514&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77953314514&partnerID=8YFLogxK
U2 - 10.1021/ja103233a
DO - 10.1021/ja103233a
M3 - Article
VL - 132
SP - 7868
EP - 7869
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 23
ER -